AI Article Synopsis

  • There are 11 lytic transglycosylases in Pseudomonas aeruginosa that are involved in breaking down the bacterial cell wall for recycling and repair, but their specific functions are not fully known.
  • Research reveals that SltB3 is an exolytic lytic transglycosylase that can recognize at least four sugars and can process a larger substrate made of 20 sugars, ultimately producing a specific compound.
  • The study presents the first X-ray structure of SltB3, showing it has four domains arranged in a circular shape, allowing the peptidoglycan substrate to pass through while it is being processed.

Article Abstract

A family of 11 lytic transglycosylases in Pseudomonas aeruginosa, an opportunistic human pathogen, turn over the polymeric bacterial cell wall in the course of its recycling, repair, and maturation. The functions of these enzymes are not fully understood. We disclose herein that SltB3 of P. aeruginosa is an exolytic lytic transglycosylase. We characterize its reaction and its products by the use of peptidoglycan-based molecules. The enzyme recognizes a minimum of four sugars in its substrate but can process a substrate comprised of a peptidoglycan of 20 sugars. The ultimate product of the reaction is N-acetylglucosamine-1,6-anhydro-N-acetylmuramic acid. The X-ray structure of this enzyme is reported for the first time. The enzyme is comprised of four domains, arranged within an annular conformation. The polymeric linear peptidoglycan substrate threads through the opening of the annulus, as it experiences turnover.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5436585PMC
http://dx.doi.org/10.1021/acschembio.6b00194DOI Listing

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